3C2V
Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae complexed with PRPP and the inhibitor phthalate
Summary for 3C2V
| Entry DOI | 10.2210/pdb3c2v/pdb |
| Related | 3C2D 3C2E 3C2F 3C2O 3C2R |
| Descriptor | Nicotinate-nucleotide pyrophosphorylase, 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose, PHTHALIC ACID, ... (4 entities in total) |
| Functional Keywords | qprtase, prtase, bna6, quinolinate, phthalate, prpp, cytoplasm, glycosyltransferase, nucleus, pyridine nucleotide biosynthesis, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Cytoplasm : P43619 |
| Total number of polymer chains | 1 |
| Total formula weight | 32826.92 |
| Authors | di Luccio, E.,Wilson, D.K. (deposition date: 2008-01-25, release date: 2008-04-01, Last modification date: 2024-02-21) |
| Primary citation | di Luccio, E.,Wilson, D.K. Comprehensive X-ray Structural Studies of the Quinolinate Phosphoribosyl Transferase (BNA6) from Saccharomyces cerevisiae. Biochemistry, 47:4039-4050, 2008 Cited by PubMed Abstract: Quinolinic acid phosphoribosyl transferase (QAPRTase, EC 2.4.2.19) is a 32 kDa enzyme encoded by the BNA6 gene in yeast and catalyzes the formation of nicotinate mononucleotide from quinolinate and 5-phosphoribosyl-1-pyrophosphate (PRPP). QAPRTase plays a key role in the tryptophan degradation pathway via kynurenine, leading to the de novo biosynthesis of NAD (+) and clearing the neurotoxin quinolinate. To improve our understanding of the specificity of the eukaryotic enzyme and the course of events associated with catalysis, we have determined the crystal structures of the apo and singly bound forms with the substrates quinolinate and PRPP. This reveals that the enzyme folds in a manner similar to that of various prokaryotic forms which are approximately 30% identical in sequence. In addition, the structure of the Michaelis complex is approximated by PRPP and the quinolinate analogue phthalate bound to the active site. These results allow insight into the kinetic mechanism of QAPRTase and provide an understanding of structural diversity in the active site of the Saccharomyces cerevisiae enzyme when compared to prokaryotic homologues. PubMed: 18321072DOI: 10.1021/bi7020475 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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